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Open data
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Basic information
| Entry | Database: PDB / ID: 8xa0 | ||||||
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| Title | penton capsomer of the VZV C-capsid | ||||||
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Keywords | VIRUS / VZV / capsid structure | ||||||
| Function / homology | Function and homology informationnuclear capsid assembly / viral genome packaging / deNEDDylase activity / T=16 icosahedral viral capsid / viral tegument / symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway / deubiquitinase activity / viral DNA genome replication / chromosome organization / viral penetration into host nucleus ...nuclear capsid assembly / viral genome packaging / deNEDDylase activity / T=16 icosahedral viral capsid / viral tegument / symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway / deubiquitinase activity / viral DNA genome replication / chromosome organization / viral penetration into host nucleus / viral capsid / host cell / symbiont-mediated perturbation of host ubiquitin-like protein modification / ubiquitinyl hydrolase 1 / host cell cytoplasm / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / symbiont entry into host cell / host cell nucleus / structural molecule activity / proteolysis Similarity search - Function | ||||||
| Biological species | Human alphaherpesvirus 3 (Varicella-zoster virus) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | ||||||
Authors | Nan, W. / Lei, C. / Xiangxi, W. | ||||||
| Funding support | 1items
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Citation | Journal: Hlife / Year: 2024Title: Insights into varicella-zoster virus assembly from the B- and C-capsid at near-atomic resolution structures Authors: Cao, L. / Wang, N. / Lv, Z. / Chen, W. / Chen, Z. / Song, L. / Sha, X. / Wang, G. / Hu, Y. / Lian, X. / Cui, G. / Fan, J. / Quan, Y. / Liu, H. / Hou, H. / Wang, X. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8xa0.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8xa0.ent.gz | 1 MB | Display | PDB format |
| PDBx/mmJSON format | 8xa0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8xa0_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 8xa0_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 8xa0_validation.xml.gz | 194.6 KB | Display | |
| Data in CIF | 8xa0_validation.cif.gz | 292.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xa/8xa0 ftp://data.pdbj.org/pub/pdb/validation_reports/xa/8xa0 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 38190MC ![]() 8x9wC ![]() 8x9xC ![]() 8x9yC ![]() 8xa1C ![]() 8xa2C ![]() 8xa3C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein/peptide , 1 types, 2 molecules 2y
| #1: Protein/peptide | Mass: 5500.510 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Gene: UL36 / Production host: Homo sapiens (human)References: UniProt: P10220, ubiquitinyl hydrolase 1, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases |
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-Protein , 4 types, 8 molecules ACEFGRVZ
| #2: Protein | Mass: 152365.312 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Gene: ORF40, MCP, ORF 40, HHV3_E_SVETAgp42, HHV3_gp42, HHV3gp42 Production host: Homo sapiens (human) / References: UniProt: Q6QCL5#5: Protein | | Mass: 27729.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Production host: Homo sapiens (human)#6: Protein | | Mass: 28721.295 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Production host: Homo sapiens (human)#7: Protein | | Mass: 32268.910 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Production host: Homo sapiens (human) |
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-Capsid vertex component ... , 2 types, 3 molecules hqu
| #3: Protein | Mass: 73998.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Gene: CVC1, UL17 / Production host: Homo sapiens (human) / References: UniProt: P10201 |
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| #4: Protein | Mass: 10890.343 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human alphaherpesvirus 3 (Varicella-zoster virus)Gene: CVC2, UL25 / Production host: Homo sapiens (human) / References: UniProt: P10209 |
-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Human alphaherpesvirus 3 / Type: VIRUS / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Human alphaherpesvirus 3 (Varicella-zoster virus) |
| Details of virus | Empty: NO / Enveloped: YES / Isolate: OTHER / Type: VIRION |
| Buffer solution | pH: 7.3 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 BASE (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 417864 / Symmetry type: POINT |
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Human alphaherpesvirus 3 (Varicella-zoster virus)
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PDBj

Homo sapiens (human)
FIELD EMISSION GUN